Relevant bibliographies by topics / Type II Baeyer-Villiger monooxygenase

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Academic literature on the topic 'Type II Baeyer-Villiger monooxygenase'

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Published: 25 May 2024

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Journal articles on the topic "Type II Baeyer-Villiger monooxygenase"

1

Isupov, Michail N., Ewald Schröder, Robert P. Gibson, Jean Beecher, Giuliana Donadio, Vahid Saneei, Stephlina A. Dcunha, et al. "The oxygenating constituent of 3,6-diketocamphane monooxygenase from the CAM plasmid ofPseudomonas putida: the first crystal structure of a type II Baeyer–Villiger monooxygenase." Acta Crystallographica Section D Biological Crystallography 71, no. 11 (October 31, 2015): 2344–53. http://dx.doi.org/10.1107/s1399004715017939.

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The three-dimensional structures of the native enzyme and the FMN complex of the overexpressed form of the oxygenating component of the type II Baeyer–Villiger 3,6-diketocamphane monooxygenase have been determined to 1.9 Å resolution. The structure of this dimeric FMN-dependent enzyme, which is encoded on the large CAM plasmid ofPseudomonas putida, has been solved by a combination of multiple anomalous dispersion from a bromine crystal soak and molecular replacement using a bacterial luciferase model. The orientation of the isoalloxazine ring of the FMN cofactor in the active site of this TIM-barrel fold enzyme differs significantly from that previously observed in enzymes of the bacterial luciferase-like superfamily. The Ala77 residue is in acisconformation and forms a β-bulge at the C-terminus of β-strand 3, which is a feature observed in many proteins of this superfamily.
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2

Isupov, Michail N., Ewald Schröder, Robert P. Gibson, Jean Beecher, Giuliana Donadio, Vahid Saneei, Stephlina A. Dcunha, et al. "The oxygenating constituent of 3,6-diketocamphane monooxygenase from the CAM plasmid ofPseudomonas putida: the first crystal structure of a type II Baeyer–Villiger monooxygenase. Corrigendum." Acta Crystallographica Section D Structural Biology 74, no. 4 (April 1, 2018): 379. http://dx.doi.org/10.1107/s205979831800150x.

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3

Löwe, Jana, Olga Blifernez-Klassen, Thomas Baier, Lutz Wobbe, Olaf Kruse, and Harald Gröger. "Type II flavoprotein monooxygenase PsFMO_A from the bacterium Pimelobacter sp. Bb-B catalyzes enantioselective Baeyer-Villiger oxidations with a relaxed cofactor specificity." Journal of Biotechnology 294 (March 2019): 81–87. http://dx.doi.org/10.1016/j.jbiotec.2019.01.011.

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4

Riebel, Anette, Michael J. Fink, Marko D. Mihovilovic, and Marco W. Fraaije. "Type II Flavin-Containing Monooxygenases: A New Class of Biocatalysts that Harbors Baeyer-Villiger Monooxygenases with a Relaxed Coenzyme Specificity." ChemCatChem 6, no. 4 (October 7, 2013): 1112–17. http://dx.doi.org/10.1002/cctc.201300550.

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5

Tanner, Adam, and David J. Hopper. "Conversion of 4-Hydroxyacetophenone into 4-Phenyl Acetate by a Flavin Adenine Dinucleotide-Containing Baeyer-Villiger-Type Monooxygenase." Journal of Bacteriology 182, no. 23 (December 1, 2000): 6565–69. http://dx.doi.org/10.1128/jb.182.23.6565-6569.2000.

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ABSTRACT An arylketone monooxygenase was purified from Pseudomonas putida JD1 by ion exchange and affinity chromatography. It had the characteristics of a Baeyer-Villiger-type monooxygenase and converted its substrate, 4-hydroxyacetophenone, into 4-hydroxyphenyl acetate with the consumption of one molecule of oxygen and oxidation of one molecule of NADPH per molecule of substrate. The enzyme was a monomer with an M r of about 70,000 and contained one molecule of flavin adenine dinucleotide (FAD). The enzyme was specific for NADPH as the electron donor, and spectral studies showed rapid reduction of the FAD by NADPH but not by NADH. Other arylketones were substrates, including acetophenone and 4-hydroxypropiophenone, which were converted into phenyl acetate and 4-hydroxyphenyl propionate, respectively. The enzyme displayed Michaelis-Menten kinetics with apparent Km values of 47 μM for 4-hydroxyacetophenone, 384 μM for acetophenone, and 23 μM for 4-hydroxypropiophenone. The apparentKm value for NADPH with 4-hydroxyacetophenone as substrate was 17.5 μM. The N-terminal sequence did not show any similarity to other proteins, but an internal sequence was very similar to part of the proposed NADPH binding site in the Baeyer-Villiger monooxygenase cyclohexanone monooxygenase from anAcinetobacter sp.
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6

Niero, Mattia, Irene Righetto, Elisa Beneventi, Patrizia Polverino de Laureto, Marco Wilhelmus Fraaije, Francesco Filippini, and Elisabetta Bergantino. "Unique Features of a New Baeyer–Villiger Monooxygenase from a Halophilic Archaeon." Catalysts 10, no. 1 (January 16, 2020): 128. http://dx.doi.org/10.3390/catal10010128.

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Type I Baeyer–Villiger monooxygenases (BVMOs) are flavin-dependent monooxygenases that catalyze the oxidation of ketones to esters or lactones, a reaction otherwise performed in chemical processes by employing hazardous and toxic peracids. Even though various BVMOs are extensively studied for their promising role in industrial biotechnology, there is still a demand for enzymes that are able to retain activity at high saline concentrations. To this aim, and based on comparative in silico analyses, we cloned HtBVMO from the extremely halophilic archaeon Haloterrigena turkmenica DSM 5511. When expressed in standard mesophilic cell factories, proteins adapted to hypersaline environments often behave similarly to intrinsically disordered polypeptides. Nevertheless, we managed to express HtBVMO in Escherichia coli and could purify it as active enzyme. The enzyme was characterized in terms of its salt-dependent activity and resistance to some water–organic-solvent mixtures. Although HtBVMO does not seem suitable for industrial applications, it provides a peculiar example of an alkalophilic and halophilic BVMO characterized by an extremely negative charge. Insights into the behavior and structural properties of such salt-requiring may contribute to more efficient strategies for engineering the tuned stability and solubility of existing BVMOs.
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7

Iwaki, Hiroaki, Yoshie Hasegawa, Shaozhao Wang, Margaret M. Kayser, and Peter C. K. Lau. "Cloning and Characterization of a Gene Cluster Involved in Cyclopentanol Metabolism in Comamonas sp. Strain NCIMB 9872 and Biotransformations Effected by Escherichia coli-Expressed Cyclopentanone 1,2-Monooxygenase." Applied and Environmental Microbiology 68, no. 11 (November 2002): 5671–84. http://dx.doi.org/10.1128/aem.68.11.5671-5684.2002.

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ABSTRACT Cyclopentanone 1,2-monooxygenase, a flavoprotein produced by Pseudomonas sp. strain NCIMB 9872 upon induction by cyclopentanol or cyclopentanone (M. Griffin and P. W. Trudgill, Biochem. J. 129:595-603, 1972), has been utilized as a biocatalyst in Baeyer-Villiger oxidations. To further explore this biocatalytic potential and to discover new genes, we have cloned and sequenced a 16-kb chromosomal locus of strain 9872 that is herein reclassified as belonging to the genus Comamonas. Sequence analysis revealed a cluster of genes and six potential open reading frames designated and grouped in at least four possible transcriptional units as (orf11-orf10-orf9)-(cpnE-cpnD-orf6-cpnC)-(cpnR-cpnB-cpnA)-(orf3-orf4 [partial 3′ end]). The cpnABCDE genes encode enzymes for the five-step conversion of cyclopentanol to glutaric acid catalyzed by cyclopentanol dehydrogenase, cyclopentanone 1,2-monooxygenase, a ring-opening 5-valerolactone hydrolase, 5-hydroxyvalerate dehydrogenase, and 5-oxovalerate dehydrogenase, respectively. Inactivation of cpnB by using a lacZ-Kmr cassette resulted in a strain that was not capable of growth on cyclopentanol or cyclopentanone as a sole carbon and energy source. The presence of σ54-dependent regulatory elements in front of the divergently transcribed cpnB and cpnC genes supports the notion that cpnR is a regulatory gene of the NtrC type. Knowledge of the nucleotide sequence of the cpn genes was used to construct isopropyl-β-thio-d-galactoside-inducible clones of Escherichia coli cells that overproduce the five enzymes of the cpn pathway. The substrate specificities of CpnA and CpnB were studied in particular to evaluate the potential of these enzymes and establish the latter recombinant strain as a bioreagent for Baeyer-Villiger oxidations. Although frequently nonenantioselective, cyclopentanone 1,2-monooxygenase was found to exhibit a broader substrate range than the related cyclohexanone 1,2-monooxygenase from Acinetobacter sp. strain NCIMB 9871. However, in a few cases opposite enantioselectivity was observed between the two biocatalysts.
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8

Kostichka, Kristy, Stuart M. Thomas, Katharine J. Gibson, Vasantha Nagarajan, and Qiong Cheng. "Cloning and Characterization of a Gene Cluster for Cyclododecanone Oxidation in Rhodococcus ruber SC1." Journal of Bacteriology 183, no. 21 (November 1, 2001): 6478–86. http://dx.doi.org/10.1128/jb.183.21.6478-6486.2001.

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ABSTRACT Biological oxidation of cyclic ketones normally results in formation of the corresponding dicarboxylic acids, which are further metabolized in the cell. Rhodococcus ruber strain SC1 was isolated from an industrial wastewater bioreactor that was able to utilize cyclododecanone as the sole carbon source. A reverse genetic approach was used to isolate a 10-kb gene cluster containing all genes required for oxidative conversion of cyclododecanone to 1,12-dodecanedioic acid (DDDA). The genes required for cyclododecanone oxidation were only marginally similar to the analogous genes for cyclohexanone oxidation. The biochemical function of the enzymes encoded on the 10-kb gene cluster, the flavin monooxygenase, the lactone hydrolase, the alcohol dehydrogenase, and the aldehyde dehydrogenase, was determined in Escherichia coli based on the ability to convert cyclododecanone. Recombinant E. colistrains grown in the presence of cyclododecanone accumulated lauryl lactone, 12-hydroxylauric acid, and/or DDDA depending on the genes cloned. The cyclododecanone monooxygenase is a type 1 Baeyer-Villiger flavin monooxygenase (FAD as cofactor) and exhibited substrate specificity towards long-chain cyclic ketones (C11 to C15), which is different from the specificity of cyclohexanone monooxygenase favoring short-chain cyclic compounds (C5 to C7).
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9

Iwaki, Hiroaki, Shaozhao Wang, Stephan Grosse, Hélène Bergeron, Ayako Nagahashi, Jittiwud Lertvorachon, Jianzhong Yang, Yasuo Konishi, Yoshie Hasegawa, and Peter C. K. Lau. "Pseudomonad Cyclopentadecanone Monooxygenase Displaying an Uncommon Spectrum of Baeyer-Villiger Oxidations of Cyclic Ketones." Applied and Environmental Microbiology 72, no. 4 (April 2006): 2707–20. http://dx.doi.org/10.1128/aem.72.4.2707-2720.2006.

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ABSTRACT Baeyer-Villiger monooxygenases (BVMOs) are biocatalysts that offer the prospect of high chemo-, regio-, and enantioselectivity in the organic synthesis of lactones or esters from a variety of ketones. In this study, we have cloned, sequenced, and overexpressed in Escherichia coli a new BVMO, cyclopentadecanone monooxygenase (CpdB or CPDMO), originally derived from Pseudomonas sp. strain HI-70. The 601-residue primary structure of CpdB revealed only 29% to 50% sequence identity to those of known BVMOs. A new sequence motif, characterized by a cluster of charged residues, was identified in a subset of BVMO sequences that contain an N-terminal extension of ∼60 to 147 amino acids. The 64-kDa CPDMO enzyme was purified to apparent homogeneity, providing a specific activity of 3.94 μmol/min/mg protein and a 20% yield. CPDMO is monomeric and NADPH dependent and contains ∼1 mol flavin adenine dinucleotide per mole of protein. A deletion mutant suggested the importance of the N-terminal 54 amino acids to CPDMO activity. In addition, a Ser261Ala substitution in a Rossmann fold motif resulted in an improved stability and increased affinity of the enzyme towards NADPH compared to the wild-type enzyme (Km = 8 μM versus Km = 24 μM). Substrate profiling indicated that CPDMO is unusual among known BVMOs in being able to accommodate and oxidize both large and small ring substrates that include C11 to C15 ketones, methyl-substituted C5 and C6 ketones, and bicyclic ketones, such as decalone and β-tetralone. CPDMO has the highest affinity (Km = 5.8 μM) and the highest catalytic efficiency (k cat/Km ratio of 7.2 × 105 M−1 s−1) toward cyclopentadecanone, hence the Cpd designation. A number of whole-cell biotransformations were carried out, and as a result, CPDMO was found to have an excellent enantioselectivity (E > 200) as well as 99% S-selectivity toward 2-methylcyclohexanone for the production of 7-methyl-2-oxepanone, a potentially valuable chiral building block. Although showing a modest selectivity (E = 5.8), macrolactone formation of 15-hexadecanolide from the kinetic resolution of 2-methylcyclopentadecanone using CPDMO was also demonstrated.
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10

Tolmie, Carmien, Martha Smit, and Diederik Opperman. "Alternative Splicing of the Aflatoxin-Associated Baeyer–Villiger Monooxygenase from Aspergillus flavus: Characterisation of MoxY Isoforms." Toxins 10, no. 12 (December 5, 2018): 521. http://dx.doi.org/10.3390/toxins10120521.

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Aflatoxins are carcinogenic mycotoxins that are produced by the filamentous fungus Aspergillus flavus, a contaminant of numerous food crops. Aflatoxins are synthesised via the aflatoxin biosynthesis pathway, with the enzymes involved encoded by the aflatoxin biosynthesis gene cluster. MoxY is a type I Baeyer–Villiger monooxygenase (BVMO), responsible for the conversion of hydroxyversicolorone (HVN) and versicolorone (VN) to versiconal hemiacetal acetate (VHA) and versiconol acetate (VOAc), respectively. Using mRNA data, an intron near the C-terminus was identified that is alternatively spliced, creating two possible MoxY isoforms which exist in vivo, while analysis of the genomic DNA suggests an alternative start codon leading to possible elongation of the N-terminus. These four variants of the moxY gene were recombinantly expressed in Escherichia coli, and their activity evaluated with respect to their natural substrates HVN and VN, as well as surrogate ketone substrates. Activity of the enzyme is absolutely dependent on the additional 22 amino acid residues at the N-terminus. Two MoxY isoforms with alternative C-termini, MoxYAltN and MoxYAltNC, converted HVN and VN, in addition to a range of ketone substrates. Stability and flavin-binding data suggest that MoxYAltN is, most likely, the dominant isoform. MoxYAltNC is generated by intron splicing, in contrast to intron retention, which is the most prevalent type of alternative splicing in ascomycetes. The alternative C-termini did not alter the substrate acceptance profile, or regio- or enantioselectivity of the enzyme, but did significantly affect the solubility and stability.
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Dissertations / Theses on the topic "Type II Baeyer-Villiger monooxygenase"

1

Downey, Theresa E. "INVESTIGATING STRUCTURE AND PROTEIN-PROTEIN INTERACTIONS OF KEY POST-TYPE II PKS TAILORING ENZYMES." UKnowledge, 2014. http://uknowledge.uky.edu/pharmacy_etds/35.

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Type II polyketide synthase (PKS) produced natural products have proven to be an excellent source of pharmacologically relevant molecules due to their rich biological activities and chemical scaffolds. Type II-PKS manufactured polyketides share similar polycyclic aromatic backbones leaving their diversity to stem from various chemical additions and alterations facilitated by post-PKS tailoring enzymes. Evidence suggests that post-PKS tailoring enzymes form complexes in order to facilitate the highly orchestrated process of biosynthesis. Thus, protein-protein interactions between these enzymes must play crucial roles in their structures and functions. Despite the importance of these interactions little has been done to study them. In the mithramycin (MTM) biosynthetic pathway the Baeyer−Villiger monooxygenase (BVMO) MtmOIV and the ketoreductase MtmW form one such enzyme pair that catalyze the final two steps en route to the final product. MtmOIV oxidatively cleaves the fourth ring of the mithramycin intermediate premithramycin B (PreB) via a Baeyer−Villiger reaction, generating MTM’s characteristic tricyclic aglycone core and highly functionalized pentyl side chain at position 3. This Baeyer−Villiger reaction precedes spontaneous lactone ring opening, decarboxylation, and the final step of MTM biosynthesis, a reduction of the 4′- keto group catalyzed by the ketoreductase MtmW. Another example of co-dependent post-PKS tailoring enzymes from the gilvocarcin biosynthetic pathway is composed of GilM and GilR. These two enzymes form an unusual synergistic tailoring enzyme pair that does not function sequentially. GilM exhibits dual functionality by catalyzing the reduction of a quinone intermediate to a hydroquinone and stabilizes O-methylation and hemiacetal formation. GilM mediates its reductive catalysis through the aid of GilR that provides its covalently bound FADH(2) for the GilM reaction, through which FAD is regenerated for the next catalytic cycle. A few steps later, following glycosylation related events unique to each gilvocarcin derivative, GilR dehydrogenates the hemiacetal moiety created by GilM to establish the formation of a lactone and the final gilvocarcin chromophore. To achieve a better understanding of post-type II PKS tailoring enzymes and their protein-proteininteractions for the benefit of future combinatorial biosynthetic efforts two specific aims were devised. Specific aim 1 was to investigate the structure of MtmOIV and the role of active site residues in its catalytic mechanism. Specific aim 2 was to integrate the function of GilM and its protein-protein interactionswith GilR that lead to their synergistic activity and sharing of GilR’s bicovalently bound FAD moiety.
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Röllig, Robert. "Chemical hydride transfer for flavin dependent monooxygenases of two-component systems." Electronic Thesis or Diss., Aix-Marseille, 2021. http://www.theses.fr/2021AIXM0436.

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Le terme monooxygénases flavoprotéiques (flavoprotein monooxygenases FPMO) recouvre aussi bien des flavoenzymes formées d’une seule composante que de deux. L'indépendance fonctionnelle de la partie oxygénase de la 2,5-dicétocamphane 1,2-monooxygénase I (2,5-DKCMO), une Baeyer-Villiger monooxygénase de type II, FMN dépendante, de sa contrepartie réductase, ainsi que le mécanisme de transfert de la flavine par libre diffusion, ont été étudiés dans des réactions sans réductase mais où des analogues biomimétiques synthétiques de nicotinamide (NCB) ont été utilisés pour réduire le FMN. L'équilibre entre la réduction de la flavine et la (ré)oxydation enzymatique a été identifié comme le goulot d'étranglement du système. Dans le but de trouver des donneurs d'hydrure potentiellement rentables pour les réactions d'oxydoréduction enzymatique, des stratégies de réduction de la flavine, indépendantes des cofacteurs nicotinamide naturels et biomimétiques, ont été étudiées. La capacité d’un complexe d’iridium III à transférer des hydrures afin de réduire la flavine a été exploitée. [Cp*Ir(bpy-OMe)H]+ (Ir* (H+)), résistant au pH et à l'oxygène, a permis la réaction enzymatique de monooxygénases respectivement FMNH2 et FADH2 dépendantes, 2,5-DKCMO et la styrène monooxygénase de sphingopyxis fribergensis Kp.5.2 (SfStyA). L’utilisation du système Ir* (H+)/SfStyA a conduit à une augmentation de six fois de l’état de l’art en terme de turn over number (TON) d’un catalyseur métallique. Cependant des améliorations sont encore nécessaires pour confirmer cette approche comme un accès prometteur à une plate-forme technologique efficace et versatile, pour l’utilisation de flavoenzymes
The term flavoprotein monooxygenases (FPMO) covers two different types of flavoenzymes: single and two component oxygenases. Two component FPMOs consist of a reductase and an oxygenating enzyme. The functional independence of the oxygenase part of 2,5-diketocamphane 1,2-monooxygenase I (2,5 DKCMO), an FMN dependent type II Baeyer-Villiger monooxygenase, from the reductase counterpart, as well as the mechanism of flavin transfer by free diffusion, was investigated in a reductase-free reaction, using synthetic nicotinamide biomimetics (NCBs) for the reduction of FMN. The balance of flavin reduction and enzymatic (re)oxidation was identified as the bottleneck of the system. Aiming for potentially cost efficient hydride donors for enzymatic redox reactions, nicotinamide coenzyme and nicotinamide biomimetic independent flavin reduction strategies were investigated. The capability of the pH and oxygen robust iridium III complex [Cp*Ir(bpy-OMe)H]+ (Ir* (H+)) to transfer hydrides for flavin reduction for the enzymatic reaction of respectively FMNH2 and FADH2 dependent monooxygenases, 2,5 DKCMO and styrene monooxygenase from Sphingopyxis fribergensis Kp.5.2 (SfStyA) was exploited. The Ir* (H+)/SfStyA approach outperformed the state of the art system by six-fold in terms of turn over number of the metal catalyst. Nevertheless, the robustness of the system remains challenging, and improvements are required to establish the approach as an efficient and versatile platform technology for flavoenzymes
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